Conserved core tryptophans of FnII domains are crucial for the membranolytic and chaperone-like activities of bovine seminal plasma protein PDC-109.

Abstract:

:The fibronectin type II (FnII) domain, present in diverse vertebrate proteins, plays crucial roles in several fundamental biological processes. PDC-109, the major bovine seminal plasma protein, contains two FnII domains that bind to choline phospholipids on sperm plasma membrane and induce lipid efflux crucial for successful fertilization. PDC-109 also exhibits chaperone-like activity and protects other proteins against various types of stress. Here, we show that a core tryptophan residue is highly conserved across species in the FnII domains. Mutation of conserved tryptophan residues W47, W93, and W106 in the FnII domains of PDC-109 to alanine leads to drastic decrease or complete abolition of membrane-binding and chaperone-like activities. These observations suggest that conserved tryptophans are important for the function of FnII proteins.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Singh BP,Asthana A,Basu A,Tangirala R,Mohan Rao C,Swamy MJ

doi

10.1002/1873-3468.13617

subject

Has Abstract

pub_date

2020-02-01 00:00:00

pages

509-518

issue

3

eissn

0014-5793

issn

1873-3468

journal_volume

594

pub_type

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